Distribution of Myelin Basic Protein and P<sub>2</sub> mRNAs in Rabbit Spinal Cord Oligodendrocytes

Gillespie, C S; Trapp, Bruce D.; Colman, David; Brophy, Peter

doi:10.1111/j.1471-4159.1990.tb01204.x

Cited by 23 publications

(15 citation statements)

References 31 publications

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“…The finding of a long half-life for MBP mRNA is consistent with the observation that MBP mRNA is translocated before it is translated (Colman et al, 1982;Gillespie et al, 1990). A long half-life will allow time for the MBP mRNA to be translocated down the oligodendrocyte processes to the myelin internode.…”

Section: Discussionsupporting

confidence: 85%

Stabilization of myelin mRNAs as measured in a brain slice system

1997

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The stabilization and destabilization of myelin mRNA is increasingly recognized as a major control point in regulating myelin gene expression. A brain slice system was developed and characterized to study mRNA stability in actively myelinating oligodendrocytes. The mRNA half-life of a major CNS myelin protein, proteolipid protein (PLP), was measured to be 5 hr. The half-life of another CNS myelin protein mRNA, myelin basic protein (MBP), was measured to be greater than 12 hr. A long half-life for MBP mRNA is consistent with MBP mRNA being stable long enough to be translocated to the myelin internode where it is then translated. Using semi-quantitative reverse transcriptase-PCR, it was determined that there was no differential stabilization between the two major PLP mRNA isoforms, PLP and DM20. It was also determined that protein synthesis was required for the specific stabilization of PLP/DM20 mRNAs. Inasmuch as PLP is a major structural protein of the CNS myelin, the PLP/DM20 mRNAs have relatively short half-lives. However, the PLP/DM20 mRNAs half-lives may be increased by the action of trans-acting factors that are themselves very labile.

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Section: Discussionsupporting

confidence: 85%

Stabilization of myelin mRNAs as measured in a brain slice system

1997

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“…MBP isoforms have been shown to segregate in different regions ofthe myelinating cell after their synthesis, for instance, 14 kDa and 18.5 kDa in the membrane and oligodendrocyte processes and 17 kDa and 2 1.5 kDa in the oligodendrocyte cell body (Gillespie et al, 1990). Our findings strongly suggest that these latter two isoforms are also localized in the radial component fraction of compact myelin.…”

Section: Mbp Isoforms 215 and 170 Kda Were Increased In Radial Compsupporting

confidence: 61%

Protein and Lipid Composition of Radial Component‐Enriched CNS Myelin

Karthigasan

Kosaras

Nguyen

et al. 1994

Journal of Neurochemistry

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The radial component is a junctional complex that is believed to stabilize the apposition of myelin membranes in the internode of CNS myelin. Based on our previous finding that the radial component of compact myelin retains its structure in tissue treated with the detergent Triton X‐100, we have attempted to isolate the junctional complex from spinal cord myelin treated with this detergent. Using 0.5% Triton X‐100, our procedures yielded a fraction of isolated myelin that was enriched in well‐preserved radial component. This fraction that contained morphologically well‐defined radial component was examined by sodium dodecyl sulfate‐polyacrylamide gel electropho‐resis and immunoblotting, and TLC, and was found to be significantly and consistently enriched in the 21.5‐kDa and 17‐kDa isoforms of myelin basic protein, and in cerebro‐sides, hydroxy sulfatide, and sphingomyelin. In addition, the myelin‐associated enzyme 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase, tubulin, and actin tended to be resistant to Triton extraction. The fraction of isolated myelin that contained radial component was deficient in proteolipid protein and DM‐20, the 18.5‐and 14‐kDa isoforms of myelin basic proteins, and in the major phospholipids, phosphatidylethanolamine, phosphatidylcholine, and phosphatidylserine. Our data indicate that the radial component can be isolated and that certain myelin and cytoskeletal proteins and lipids are closely associated with it.

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“…Other studies report that the MBP isoforms segregate in different regions of the myelinating cell after their synthesis -e.g. the major isoforms (14kDa and 18.5kDa) to the membrane of oligodendrocyte processes and the minor isoforms (17kDa and 21.5kDa) to the cell body of the oligodendrocyte (Colman et al, 1982;Gillespie et al, 1990). Our current findings together with our previous ones (see above) suggest that the minor isoforms recognized specifically by Ab-MBP 215 also become incorporated within the oligodendrocyte membrane itself, and localise to the junction-free compact myelin and to the radial component, where they become enriched relative to the major MBP isoforms.…”

Section: Differential Immunolabelling Of Radial Component and Junctiomentioning

confidence: 99%

Immunolocalization of 17 and 21.5 kDa MBP isoforms in compact myelin and radial component

Karthigasan

Garvey

Ramamurthy³

et al. 1996

J Neurocytol

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Our previous biochemical analyses revealed that the levels of the minor MBP isoforms 21.5 and 17 kDa are elevated relative to the 14 and 18.5 kDa MBP isoforms in the fraction of isolated myelin of murine CNS that is enriched in interlamellar junctions (or radial component). To substantiate the localization of 21.5 and 17 kDa MBP in the myelin sheath, we used immunoelectron microscopy on thin-sections of mouse optic nerve. Two different polyclonal antibodies were used to distinguish 21.5 and 17 kDa MBP from 14 and 18.5 kDa MBP: Ab-MBP21.5, which was raised against a synthetic peptide corresponding to the exon II amino acid sequence 61-83 of mouse 21.5 kDa MBP (LKQSRSPLPSHARSRPGLCHMYK), and Ab-MBP14, which is immunoreactive to all four isoforms of mouse MBP. Our SDS-PAGE/immunoblotting demonstrated that Ab-MBP21.5, unlike Ab-MBP14, recognized only the 21.5 and 17 kDa MBP isoforms from isolated mouse CNS myelin. Immunolabelling of tissue sections indicated that Ab-MBP14 bound tenfold more to junction-free compact myelin than to radial component, whereas Ab-MBP21.5 bound about equally to the two regions of the myelin sheath. In addition, within the junction-free compact myelin, both antibodies bound nearly three fold more to the major dense line than to the intraperiod line.

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Distribution of Myelin Basic Protein and P₂ mRNAs in Rabbit Spinal Cord Oligodendrocytes

Cited by 23 publications

References 31 publications

Stabilization of myelin mRNAs as measured in a brain slice system

Stabilization of myelin mRNAs as measured in a brain slice system

Protein and Lipid Composition of Radial Component‐Enriched CNS Myelin

Immunolocalization of 17 and 21.5 kDa MBP isoforms in compact myelin and radial component

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Distribution of Myelin Basic Protein and P2 mRNAs in Rabbit Spinal Cord Oligodendrocytes

Cited by 23 publications

References 31 publications

Stabilization of myelin mRNAs as measured in a brain slice system

Stabilization of myelin mRNAs as measured in a brain slice system

Protein and Lipid Composition of Radial Component‐Enriched CNS Myelin

Immunolocalization of 17 and 21.5 kDa MBP isoforms in compact myelin and radial component

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Distribution of Myelin Basic Protein and P₂ mRNAs in Rabbit Spinal Cord Oligodendrocytes